The scope, efficiency, and practicality of making abiotic, chiral, nonstoichiometric catalysts that stimulate enzyme systems will be explored. Synthetic transacylases, carboxylases, and decarboxylases will be designed, synthesized, and tested. The object is to stimulate the enzyme systems' abilities to catalyze organic reactions. Rapid rates, high yields, high turnover, high substrate specificity, and high stereo-specificity are the properties most desired. Host compounds with convergent binding sites and chiral barriers will be catalysts, and guest compounds with divergent binding sites will be reactants. The achiral reaction centers of guests by complexation with designed chiral hosts will be converted to prochiral centers in the complexes which upon reaction will become chiral centers in the product. The configurational direction of the chiral bias and the degree of asymmetric induction will be predicted and correlated with space-filling molecular models of host-guest complexes whose structures are determined by X-ray or 1H NMR spectroscopy. The catalysis will be made nonstoichiometric through rate increases associated with guest-activation by collection (sometimes by phase-transfer) and by orientation.